Structure of PDB 6ccz Chain A Binding Site BS05
Receptor Information
>6ccz Chain A (length=443) Species:
3880
(Medicago truncatula) [
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FLDYGLSEADPDVHAIINKEKDRQFRSLELIASENFTSKAVMEAVGSCLT
NKYSEGLPGKRYYGGNEHIDELEILCQQRALAAFHLDGDKWGVNVQPLSG
SPANFAVYTAILKPHDRIMGLDLPHGGHLSHGFRVSGTSIYFESMPYRLD
ESTGVIDYDMLEKTAALFRPKLIIAGASAYPRDIDYARFRKIADSVGAFL
MMDMAHVSGLIAASVLADPFEFVDIVTTTTHKSLRGPRGGMIFFKKDAVH
GVDLESAINNAVFPGLQGGPHNHTIGGLAVCLKYAQSPDFKNYQNQVVAN
CRALANRLVEHEYKLVSGGSDNHLVLVDLRPSGIDGARVEKILDMASITL
NKNSVPGDVPGGIRIGSPAMTTRGLGEKEFELIADLIHEGVRISLEAKSL
VSGTKVQDFLNFVLAPEFPLGDKVSNLRRKVEALATQYPIPGV
Ligand information
Ligand ID
SEY
InChI
InChI=1S/CH4N2Se/c2-1(3)4/h(H4,2,3,4)
InChIKey
IYKVLICPFCEZOF-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.370
NC(N)=[Se]
OpenEye OEToolkits 1.7.6
C(=[Se])(N)N
ACDLabs 12.01
[Se]=C(N)N
Formula
C H4 N2 Se
Name
selenourea
ChEMBL
CHEMBL3187603
DrugBank
ZINC
PDB chain
6ccz Chain A Residue 607 [
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Receptor-Ligand Complex Structure
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PDB
6ccz
Chloroplastic Serine Hydroxymethyltransferase FromMedicago truncatula: A Structural Characterization.
Resolution
2.14 Å
Binding residue
(original residue number in PDB)
N345 F349
Binding residue
(residue number reindexed from 1)
N259 F263
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
Y134 E136 D289 T315 K318 R324
Catalytic site (residue number reindexed from 1)
Y53 E55 D203 T229 K232 R238
Enzyme Commision number
2.1.2.1
: glycine hydroxymethyltransferase.
Gene Ontology
Molecular Function
GO:0004372
glycine hydroxymethyltransferase activity
GO:0030170
pyridoxal phosphate binding
Biological Process
GO:0019264
glycine biosynthetic process from serine
GO:0035999
tetrahydrofolate interconversion
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:6ccz
,
PDBe:6ccz
,
PDBj:6ccz
PDBsum
6ccz
PubMed
29868052
UniProt
G7ILW0
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